(data stored in ACNUC1104 zone)

SWISSPROT: D3UY23_XENBS

ID   D3UY23_XENBS            Unreviewed;       651 AA.
AC   D3UY23;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|HAMAP-Rule:MF_01123};
DE            Short=AcCoA synthetase {ECO:0000256|HAMAP-Rule:MF_01123};
DE            Short=Acs {ECO:0000256|HAMAP-Rule:MF_01123};
DE            EC=6.2.1.1 {ECO:0000256|HAMAP-Rule:MF_01123};
DE   AltName: Full=Acetate--CoA ligase {ECO:0000256|HAMAP-Rule:MF_01123};
DE   AltName: Full=Acyl-activating enzyme {ECO:0000256|HAMAP-Rule:MF_01123};
GN   Name=acs {ECO:0000256|HAMAP-Rule:MF_01123,
GN   ECO:0000313|EMBL:CBJ79201.1};
GN   OrderedLocusNames=XBJ1_0050 {ECO:0000313|EMBL:CBJ79201.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79201.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79201.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79201.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA
CC       (AcCoA), an essential intermediate at the junction of anabolic and
CC       catabolic pathways. Acs undergoes a two-step reaction. In the
CC       first half reaction, Acs combines acetate with ATP to form acetyl-
CC       adenylate (AcAMP) intermediate. In the second half reaction, it
CC       can then transfer the acetyl group from AcAMP to the sulfhydryl
CC       group of CoA, forming the product AcCoA. {ECO:0000256|HAMAP-
CC       Rule:MF_01123}.
CC   -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA
CC       (AcCoA), an essential intermediate at the junction of anabolic and
CC       catabolic pathways. AcsA undergoes a two-step reaction. In the
CC       first half reaction, AcsA combines acetate with ATP to form
CC       acetyl-adenylate (AcAMP) intermediate. In the second half
CC       reaction, it can then transfer the acetyl group from AcAMP to the
CC       sulfhydryl group of CoA, forming the product AcCoA.
CC       {ECO:0000256|SAAS:SAAS00711888}.
CC   -!- FUNCTION: Enables the cell to use acetate during aerobic growth to
CC       generate energy via the TCA cycle, and biosynthetic compounds via
CC       the glyoxylate shunt. Acetylates CheY, the response regulator
CC       involved in flagellar movement and chemotaxis. {ECO:0000256|HAMAP-
CC       Rule:MF_01123}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:456215; EC=6.2.1.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01123};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01123, ECO:0000256|SAAS:SAAS00711884};
CC   -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC       activates the enzyme. {ECO:0000256|HAMAP-Rule:MF_01123}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. {ECO:0000256|HAMAP-Rule:MF_01123}.
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DR   EMBL; FN667741; CBJ79201.1; -; Genomic_DNA.
DR   RefSeq; WP_012986674.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0050; -.
DR   EnsemblBacteria; CBJ79201; CBJ79201; XBJ1_0050.
DR   GeneID; 8829678; -.
DR   KEGG; xbo:XBJ1_0050; -.
DR   PATRIC; fig|406818.4.peg.43; -.
DR   eggNOG; ENOG4108IQF; Bacteria.
DR   eggNOG; COG0365; LUCA.
DR   HOGENOM; HOG000229981; -.
DR   KO; K01895; -.
DR   OMA; DHWWHDL; -.
DR   BioCyc; XBOV406818:XBJ1_RS00230-MONOMER; -.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:UniProtKB-UniRule.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR   CDD; cd05966; ACS; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   HAMAP; MF_01123; Ac_CoA_synth; 1.
DR   InterPro; IPR011904; Ac_CoA_lig.
DR   InterPro; IPR032387; ACAS_N.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; AMP-dep_Synthh-like_sf.
DR   Pfam; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UY23.
DR   SWISS-2DPAGE; D3UY23.
KW   Acetylation {ECO:0000256|HAMAP-Rule:MF_01123};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01123, ECO:0000313|EMBL:CBJ79201.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01123,
KW   ECO:0000256|SAAS:SAAS00711869};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01123,
KW   ECO:0000256|SAAS:SAAS00711886};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
FT   DOMAIN       24     81       ACAS_N. {ECO:0000259|Pfam:PF16177}.
FT   DOMAIN       83    522       AMP-binding. {ECO:0000259|Pfam:PF00501}.
FT   DOMAIN      531    609       AMP-binding_C. {ECO:0000259|Pfam:
FT                                PF13193}.
FT   NP_BIND     387    389       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   NP_BIND     411    416       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   REGION      191    194       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01123}.
FT   METAL       537    537       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   METAL       539    539       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   METAL       542    542       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     311    311       Coenzyme A. {ECO:0000256|HAMAP-Rule:
FT                                MF_01123}.
FT   BINDING     335    335       Coenzyme A. {ECO:0000256|HAMAP-Rule:
FT                                MF_01123}.
FT   BINDING     500    500       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     515    515       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     523    523       Coenzyme A; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     526    526       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     584    584       Coenzyme A. {ECO:0000256|HAMAP-Rule:
FT                                MF_01123}.
FT   MOD_RES     609    609       N6-acetyllysine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01123}.
SQ   SEQUENCE   651 AA;  72315 MW;  B5C00BDBA2B0B935 CRC64;
     MTQIIKHLIP ADIAETALIS KQQYLQDYQW SLQDPEAFWS EKGKIVDWIK PYTQVKNTSF
     DPGHVSIRWF EDGTLNLSAN CLDRHLQERG EQTAIIWEGD NPAESKHVTY RELYHDVCQF
     ANVLKKLDVK KGDVVAIYMP MVPEAAVAML ACTRVGAIHS VIFGGFSPDA IAGRVIDSNA
     KLIITADEGI RAGRVIPLKK NVDEALSNPA VTDVVNVVVF KRTGNTKSWQ EGRDLWWHEL
     IENVSTDCPA EEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYASLTFK YTFDYRPGEI
     YWCTADIGWV TGHSYLLYGP LSCGATSLMF EGVPNYPDVN RLCQIVDKHQ VNIIYTAPTA
     IRALMAEGDK AIEGTKRTSL RIMGSVGEPI NPEAWEWYYR KIGNSKCPIV DTWWQTETGG
     FMITPLPGAV DLKPGSATLP FFGISPALVG NSGEPLTGEC EGNLVITDSW PGQARTLFGD
     HERFEQTYFS TFKGMYFSGD GARRDEDGYY WITGRVDDVL NISGHRLGTA EIESALVSHP
     KIAEAAVVGI PHHIKGQAIY AYVTLNHGEE PSPDLYTEVR NWVRKEIGPI ATPDILHWTD
     SLPKTRSGKI MRRILRKIAS GDTSNLGDTS TLADPGVVEK LLEEKQSMNM T
//

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